Hyaluronidase

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== Function ==
== Function ==
'''Hyaluronidase''' (HU) hydrolyzes complex carbohydrates such as hyaluronan which is part of the extracellular matrix. The hydrolysis increases tissue permeability.
'''Hyaluronidase''' (HU) hydrolyzes complex carbohydrates such as hyaluronan which is part of the extracellular matrix. The hydrolysis increases tissue permeability.
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== Relevance ==
 
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HU is used in medicine to speed drug delivery. Hyaluronic acid (HUA) is a popular dermal filler material.
 
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|[[Image:Hyal reaction.jpg|thumb|right|'''Hyaluronidase cleaves the β1,4-glycosidic bond of the glycosaminoglycan hyaluronan''' |400px]]
|[[Image:Hyal reaction.jpg|thumb|right|'''Hyaluronidase cleaves the β1,4-glycosidic bond of the glycosaminoglycan hyaluronan''' |400px]]
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== Relevance ==
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HU is used in medicine to speed drug delivery. Hyaluronic acid (HUA) is a popular dermal filler material.
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== Structural highlights ==
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HU structure contains an N-terminal, linker and C-terminal domains. The active site is in a cleft in the N-terminal domain. Two HUA molecules are bound in the active site making contacts with some HU residues and multiple contacts with water molecules<ref>PMID:10843845</ref>.
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Revision as of 08:45, 27 March 2016

Hyaluronidase complex with hyaluronic acid disaccharide and dimethylarsinate, 1c82

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3D structures of hyaluronidase

Updated on 27-March-2016

Reference

Structure of human hyaluronidase-1, a hyaluronan hydrolyzing enzyme involved in tumor growth and angiogenesis., Chao KL, Muthukumar L, Herzberg O, Biochemistry. 2007 Jun 12;46(23):6911-20. Epub 2007 May 16. PMID:17503783


Created with the participation of Osnat Herzberg, Eran Hodis, Joel L. Sussman, Jaime Prilusky.

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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